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Sequential digestion with Trypsin and Elastase in cross-linking/mass spectrometry

By Therese Dau, Kapil Gupta, Imre Berger, Juri Rappsilber

Posted 23 Oct 2018
bioRxiv DOI: 10.1101/450981 (published DOI: 10.1021/acs.analchem.8b05222)

Cross-linking/mass spectrometry has become an important approach for studying protein structures and protein-protein interactions. The amino acid composition of some protein regions impedes the detection of cross-linked residues, although it would yield invaluable information for protein modelling. Here, we report on a sequential digestion strategy with trypsin and elastase to penetrate regions with a low density of trypsin cleavage sites. We exploited intrinsic substrate recognition properties of elastase to specifically target larger tryptic peptides. Our application of this protocol to the TAF4-12 complex allowed us to identify cross-links in previously inaccessible regions.

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